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Structural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation.

Abstract：

:Aminoglycoside phosphotransferases represent a broad class of enzymes that promote bacterial resistance to aminoglycoside antibiotics via the phosphorylation of hydroxyl groups in the latter. Here we report the spatial structure of the 3'-aminoglycoside phosphotransferase of novel VIII class (AphVIII) solved by X-ray diffraction method with a resolution of 2.15 Å. Deep analysis of APHVIII structure and its comparison with known structures of aminoglycoside phosphotransferases of various types reveals that AphVIII has a typical two-domain fold and, however, possesses some unique characteristics that distinguish the enzyme from its known homologues. The most important difference is the presence of the activation loop with unique Ser146 residue. We demonstrate that in the apo-state of the enzyme the activation loop does not interact with other parts of the enzyme and seems to adopt catalytically competent state only after substrate binding.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Boyko KM,Gorbacheva MA,Korzhenevskiy DA,Alekseeva MG,Mavletova DA,Zakharevich NV,Elizarov SM,Rudakova NN,Danilenko VN,Popov VO

doi

10.1016/j.bbrc.2016.06.097

subject

Has Abstract

pub_date

2016-09-02 00:00:00

pages

595-601

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)31017-8

journal_volume

477

pub_type

杂志文章

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